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X-ray Crystallography

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...

$X-ray Diffraction of Biological Samples$ 01:10

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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are scattered by the electron clouds around the sample atoms. The X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...

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Related Experiment Video

Updated: Jun 26, 2026

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

The Biomolecular Crystallization Database Version 4: expanded content and new features.

Michael Tung¹, D Travis Gallagher

¹Center for Advanced Research in Biotechnology/National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA.

Acta Crystallographica. Section D, Biological Crystallography

|January 21, 2009

Summary

This summary is machine-generated.

The Biological Macromolecular Crystallization Database (BMCD) now offers enhanced search capabilities and expanded data, including macromolecule sequences. This updated resource aids researchers in analyzing protein crystallization for scientific discovery.

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Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

The Biological Macromolecular Crystallization Database (BMCD) has served as a vital resource for crystallographic data since 1988.
It archives information on crystal growth for proteins and other biological macromolecules.

Purpose of the Study:

To update and enhance the BMCD with expanded content and improved search functionalities.
To facilitate more elaborate analysis of factors influencing biological macromolecular crystallization.

Main Methods:

Expanded the BMCD content to include 14,372 crystal entries and macromolecule sequences.
Integrated Java-based Lucene query language for detailed parameter searching, including numeric ranges.
Developed tools for importing and handling data from the RCSB Protein Data Bank.

Main Results:

The updated database, BMCD version 4.02 (BMCD4), now includes comprehensive macromolecule sequence data.
Enhanced search capabilities allow for detailed analysis of relationships between protein properties, crystallization conditions, and crystal characteristics.
The resource remains freely accessible online.

Conclusions:

The enhanced BMCD4 provides a powerful, updated platform for researchers.
Improved data and search functionalities will accelerate the design of crystal-growth strategies and scientific analysis.